Serine proteases: subtilisins
Subtilisins are a family of alkaline serine proteases,
generally secreted by a variety of Bacillus species
(Siezen & Leunissen 1997). They catalyse the
hydrolysis of peptide and ester bonds through the
formation of an acyl-enzyme intermediate. Subtilisins
are made as preproprotein precursors (Wells
et al. 1983). The NH2-terminal prepeptide, of 29
amino acid residues is the signal peptide required for
secretion of prosubtilisin across the plasma membrane.
The propeptide of 77 amino acids, located
between the prepeptide and mature sequence, acts as
an intramolecular chaperone required for the correct
folding of mature enzyme in active form (Stahl &
Ferrari 1984; Wong & Doi 1986; Ikemura et al. 1987;Ikemura & Inouye 1988)
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